X-ray diffraction
2.2Å resolution

Crystal Structure of Human PCNA in complex with a TRAIP peptide


Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-146053 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Proliferating cell nuclear antigen Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 253 amino acids
Theoretical weight: 27.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P12004 (Residues: 2-254; Coverage: 97%)
Gene name: PCNA
Sequence domains:
Structure domains: Proliferating Cell Nuclear Antigen
E3 ubiquitin-protein ligase TRAIP Chains: D, E
Molecule details ›
Chains: D, E
Length: 12 amino acids
Theoretical weight: 1.43 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q9BWF2 (Residues: 459-469; Coverage: 2%)
Gene names: RNF206, TRAIP, TRIP
Molecule details ›
Chain: F
Length: 5 amino acids
Theoretical weight: 345 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P65
Unit cell:
a: 84.36Å b: 84.36Å c: 210.862Å
α: 90° β: 90° γ: 120°
R R work R free
0.204 0.204 0.234
Expression systems:
  • Escherichia coli
  • Not provided